Effects of the Acid- and Alkali-Aided Processes on Bighead Carp (Aristichthys nobilis) Muscle Proteins

REFERENCES

• Azadian, M.; Moosavi-Nasab, M.; Abedi, E. Comparison of Functional Properties and SDS-PAGE Patterns Between Fish Protein Isolate and Surimi Produced from Silver Carp. European Food Research and Technology 2012, 235 (1), 83–90.
   Web of Science ®Google Scholar
• Nolsøe, H.; Undeland, I. The Acid and Alkaline Solubilization Process for the Isolation of Muscle Proteins: State of the Art. Food and Bioprocess Technology 2008, 2 (1), 1–27.
   Web of Science ®Google Scholar
• Liu, Z.Y.; et al. Fermentation of Bighead Carp (Aristichthys Nobilis) Surimi and the Characteristics of Fermented Bighead Carp Surimi Products. Journal of the Science of Food and Agriculture 2009, 89 (3), 511–516.
   Web of Science ®Google Scholar
• FAO. Cultured Aquatic Species Information Programme Hypophthalmichthys nobilis (Richardson, 1845), 2014.
   Google Scholar
• Rawdkuen, S.; et al. Biochemical and Gelling Properties of Tilapia Surimi and Protein Recovered Using An Acid-Alkaline Process. Food Chemistry 2009, 112 (1), 112–119.
   Web of Science ®Google Scholar
• Kristinsson, H.G.; et al. A Comparative Study Between Acid- and Alkali-Aided Processing and Surimi Processing for the Recovery of Proteins from Channel Catfish Muscle. Journal of Food Science 2005, 70 (4), C298–C306.
   Web of Science ®Google Scholar
• Hultin, H.O.; Kelleher, S.D. Surimi Processing from Dark Muscle Fish. In Surimi and Surimi Seafood; Park, J.W.; Ed.; Marcel Dekker: New York, NY, 2000.
   Google Scholar
• Kristinsson, H.G.; Liang, Y. Effect of pH-Shift Processing and Surimi Processing on Atlantic Croaker (Micropogonias Undulates) Muscle Proteins. Journal of Food Science 2006, 71 (5), C304–C312.
   Web of Science ®Google Scholar
• Ingadottir, B.; Kristinsson, H.G. Gelation of Protein Isolates Extracted from Tilapia Light Muscle by pH Shift Processing. Food Chemistry 2010, 118 (3), 789–798.
   Web of Science ®Google Scholar
• Taskaya, L.; Chen, Y.-C.; Jaczynski, J. Color Improvement by Titanium Dioxide and Its Effect on Gelation and Texture of Proteins Recovered from Whole Fish Using Isoelectric Solubilization/Precipitation. LWT–Food Science and Technology 2010, 43 (3), 401–408.
   Web of Science ®Google Scholar
• AOAC. Official Methods of Analysis, 17th Ed. ; Association of Official Analytical Chemists: Washington, DC, 2000.
   Google Scholar
• Kim, Y.S.; Park, J.W.; Choi, Y.J. New Approaches for the Effective Recovery of Fish Proteins and Their Physicochemical Characteristics. Fisheries Science 2003, 69 (6), 1231–1239.
   Web of Science ®Google Scholar
• Pons, M. Instrumental Texture Profile Analysis with Particular Reference to Gelled Systems. Journal of Texture Studies 1996, 27 (6), 597–624.
   Web of Science ®Google Scholar
• Gómez-Guillén, M.C.; Borderı́as, A.J.; Montero, P. Chemical Interactions of Nonmuscle Proteins in the Network of Sardine (Sardina Pilchardus) Muscle Gels. LWT–Food Science and Technology 1997, 30 (6), 602–608.
   Web of Science ®Google Scholar
• Kruger, N.J. The Bradford Method for Protein Quantitation. Methods in Molecular Biology 1994, 32, 9–15.
   PubMedGoogle Scholar
• Undeland, I.; Kelleher, S.D.; Hultin, H.O. Recovery of Functional Proteins from Herring (Clupea Harengus) Light Muscle by An Acid Or Alkaline Solubilization Process. Journal of Agricultural and Food Chemistry 2002, 50 (25), 7371–7379.
   PubMed Web of Science ®Google Scholar
• Choi, Y.J.; Park, J.W. Acid-Aided Protein Recovery from Enzyme-Rich Pacific Whiting. Journal of Food Science 2002, 67 (8), 2962–2967.
   Web of Science ®Google Scholar
• Kristinsson, H.G.; Ingadottir, B. Recovery and Properties of Muscle Proteins Extracted from Tilapia (Oreochromis Niloticus) Light Muscle by pH Shift Processing. Journal of Food Science 2006, 71 (3), E132–E141.
   Web of Science ®Google Scholar
• Szczesniak, A.S. Texture Is a Sensory Property. Food Quality and Preference 2002, 13 (4), 215–225.
   Web of Science ®Google Scholar
• An, H.; Peters, M.Y.; Seymour, T.A. Roles of Endogenous Enzymes in Surimi Gelation. Trends in Food Science and Technology 1996, 7, 321–327.
   Web of Science ®Google Scholar
• Kristinsson, H.G.; Hultin, H.O. Changes in Conformation and Subunit Assembly of Cod Myosin at Low and High pH and After Subsequent Refolding. Journal of Agricultural and Food Chemistry 2003, 51 (24), 7187–7196.
   PubMed Web of Science ®Google Scholar
• Chen, Y.C.; Jaczynski, J. Protein Recovery from Rainbow Trout (Oncorhynchus Mykiss) Processing Byproducts Via Isoelectric Swolubilization/Precipitation and Its Gelation Properties As Affected by Functional Additives. Journal of Agricultural and Food Chemistry 2007, 55 (22), 9079–9088.
   PubMed Web of Science ®Google Scholar
• Beas, V.E.; et al. Thermal Denaturation in Fish Muscle Proteins During Gelling: Effect of Spawning Condition. Journal of Food Science 1991, 56 (2), 281–284.
   Web of Science ®Google Scholar
• Yongsawatdigul, J.; Park, J.W. Effects of Alkali and Acid Solubilization on Gelation Characteristics of Rockfish Muscle Proteins. Journal of Food Science 2004, 69 (7), C499–C505.
   Web of Science ®Google Scholar
• Hwang, J.S.; Lai, K.M.; Hsu, K.C. Changes in Textural and Rheological Properties of Gels from Tilapia Muscle Proteins Induced by High Pressure and Setting. Food Chemistry 2007, 104 (2), 746–753.
   Web of Science ®Google Scholar
• Yamamoto, K.; Miura, T.; Yasui, T. Gelation of Myosin Filament Under High Hydrostatic Pressure. Food Structure 1990, 9, 269–277.
   Web of Science ®Google Scholar
• Chaijan, M.; et al. Physicochemical Properties, Gel-Forming Ability, and Myoglobin Content of Sardine (Sardinella Gibbosa) and Mackerel (Rastrelliger Kanagurta) Surimi Produced by Conventional Method and Alkaline Solubilisation Process. European Food Research and Technology 2005, 222(1–2), 58–63.
   Web of Science ®Google Scholar
• Park, J.W. Surimi and Surimi Seafood, 2nd Ed; CRC Press: Boca Raton, FL, 2005.
   Google Scholar
• Lanier, T.C. Surimi Gelation Chemistry. In Surimi and Surimi Seafood; Park, J.W.; Ed.; Marcel Dekker: New York, NY, 2000; 237–265.
   Google Scholar
• Monahan, F.J.; German, J.B.; Kinsella, J.E. Effect of pH and Temperature on Protein Unfolding and Thiol/Disulfide Interchange Reactions During Heat-Induced Gelation of Whey Proteins. Journal of Agricultural and Food Chemistry 1995, 43, 46–52.
   Web of Science ®Google Scholar
• Choi, S.M.; Ma, C.Y. Structural Characterization of Globulin from Common Buckwheat (Fagopyrum Esculentum Moench) Using Circular Dichroism and Raman Spectroscopy. Food Chemistry 2007, 102 (1), 150–160.
   Web of Science ®Google Scholar
• Greenfield, N.J. Applications of Circular Dichroism in Protein and Peptide Analysis. Trends in Analytical Chemistry 1999, 18 (4), 236–244.
   Web of Science ®Google Scholar
• Harrington, W.F.; Rodgers, M.E. Myosin. Annual Review of Biochemistry 1984, 53, 35–73.
   PubMed Web of Science ®Google Scholar
• Damodaran, S. Aminoacids, Peptides, and Proteins. In Food Chemistry; Fennema, O.R.; Ed.; Marcel Dekker: New York, NY, 1996; 321–429.
   Google Scholar
• Liu, R.; et al. Effect of pH on the Gel Properties and Secondary Structure of Fish Myosin. Food Chemistry 2010, 121 (1), 196–202.
   Web of Science ®Google Scholar
• Yuan, C.; et al. Structural Stability of Myosin Rod from Silver Carp As Affected by Season. Journal of Food Science 2011, 76 (5), C686–C693.
   PubMed Web of Science ®Google Scholar